{Reference Type}: Journal Article
{Author}: Bayramoglu, Gulay; Akbulut, Aydin; Arica, M. Yakup
{Year}: 2013
{Title}: Immobilization of tyrosinase on modified diatom biosilica: Enzymatic removal of phenolic compounds from aqueous solution
{Tag}: 0
{Star}: 0
{Journal}: JOURNAL OF HAZARDOUS MATERIALS
{Volume}: 244
{Pages}: 528-536
{ISBN/ISSN}: 0304-3894
{Keywords}: POLYPHENOL OXIDASE; AGARICUS-BISPORUS; CHEMICAL-MODIFICATION; CATALYTIC-PROPERTIES; MUSHROOM TYROSINASE; POLY(GMA-MMA) BEADS; DYE DEGRADATION; BED REACTOR; LACCASE; GLUTARALDEHYDE; Diatoms; Modification; Tyrosinase; Enzyme immobilization; Phenolic compounds; Biodegradation
{Abstract}: Acid and plasma treated diatom-biosilica particles, were modified with 3-aminopropyl triethoxysilane (APTES), and activated with glutaraldehyde. Then, tyrosinase was immobilized onto the pre-activated biosilica by covalent bonding. The biosilica properties were determined using SEM, and FTIR. The enzyme system has been characterized as a function of pH, temperature and substrate concentration. Optimum pH of the free and immobilized enzyme was found to be pH 7.0. Optimum temperatures of the free and immobilized enzymes were determined as 35 and 45 degrees C respectively. The biodegradation of phenolic compounds (i.e., phenol, para-cresol and phenyl acetate) has been studied by means of immobilized tyrosinase in a batch system. The immobilized tyrosinase retained about 74% of its original activity after 10 times repeated use in the batch system. Moreover, the storage stability of the tyrosinase-biosilica system resulted excellent, since they maintained more than 67% of the initial activity after eighth week storage. Highly porous structure of biosilica can provide large surface area for immobilization of high quantity enzyme. The porous structure of the biosilica can decrease diffusion limitation both substrate phenols and their products. Finally, the immobilized tyrosinase was used in a batch system for degradation of three different phenols. (c) 2012 Elsevier B.V. All rights reserved.
{Author Address}: Gazi Univ, Fac Sci, Biochem Proc & Biomat Res Lab, TR-06500 Ankara, Turkey; Hacettepe Univ, Dept Environm Sci, Inst Nat & Appl Sci, TR-06800 Ankara, Turkey; Gazi Univ, Fac Sci, Biochem Proc & Biomat Res Lab, TR-06500 Ankara, Turkey
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Turkey; Turkey

{Reference Type}: Journal Article
{Author}: Nitha, B.; Fijesh, P. V.; Janardhanan, K. K.
{Year}: 2013
{Title}: Hepatoprotective activity of cultured mycelium of Morel mushroom, Morchella esculenta
{Tag}: 0
{Star}: 0
{Journal}: EXPERIMENTAL AND TOXICOLOGIC PATHOLOGY
{Volume}: 65
{Issue}: 1-2
{Pages}: 105-112
{ISBN/ISSN}: 0940-2993
{Keywords}: CARBON-TETRACHLORIDE; LIPID-PEROXIDATION; TREATED RATS; LIVER-INJURY; ANTIOXIDANT; GLUTATHIONE; EXTRACT; ENZYMES; SERUM; MICE; Carbon tetrachloride; Ethanol; Hepatoprotection; Medicinal mushrooms; Morchella esculenta; Mushroom mycelium
{Abstract}: The hepatoprotective activity of cultured mycelium of morel mushroom Morchella esculenta against CCl4 and ethanol induced chronic hepatotoxicity was investigated. Hepatotoxicity was induced by challenging the animals with CCl4 (1:5, v/v, 3.75 ml/kg body weight, i.p., 30 doses) and ethanol (36%, v/v, 6 ml/animal, p.o., 35 doses) and the extract was administered at two concentrations (250 and 500 mg/kg body weight). Hepatoprotection was evaluated by determining the activities of liver function marker enzymes and antioxidant status of liver and also by histopathological observations of liver tissue. Administration of both ethanol and CCl4 elevated the levels of liver function enzymes, GOT, GPT and ALP in serum drastically. The treatment with the extract decreased the elevated serum GOT, GPT and ALP activities in a dose dependent manner. The extract also restored the depleted levels of antioxidants in liver consequent to CCl4 and ethanol challenge. The results indicated that aqueous-ethanolic extract of M. esculenta mycelium possessed significant hepatoprotective activity. The conclusion is also supported by the biochemical determinations and histopathological observations. The findings thus suggest the potential therapeutic use of morel mushroom mycelium as a novel hepatoprotective agent. (C) 2011 Elsevier GmbH. All rights reserved.
{Author Address}: Amala Canc Res Ctr, Dept Microbiol, Trichur 680555, Kerala, India; Amala Canc Res Ctr, Dept Microbiol, Trichur 680555, Kerala, India; Amala Canc Res Ctr, Dept Microbiol, Trichur 680555, Kerala, India
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: India

{Reference Type}: Journal Article
{Author}: Su, C. H.; Lai, M. N.; Ng, L. T.
{Year}: 2013
{Title}: Inhibitory effects of medicinal mushrooms on alpha-amylase and alpha-glucosidase   - enzymes related to hyperglycemia
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=23396484&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Food Funct
{Volume}: 4
{Issue}: 4
{Pages}: 644-9
{DOI}: 10.1039/c3fo30376d
{Date Displayed}: 2013 Apr 25
{Date}: 2013-04-25
{Type of Work}: Journal Article
{Accession Number}: 23396484
{Abstract}: In Asia, medicinal mushrooms have been popularly used as folk medicine and functional foods. In this study, our aim was to examine the inhibitory effects of six medicinal mushrooms on key enzymes (alpha-amylase and alpha-glucosidase) related to hyperglycemia; chemical profiles of bioactive extracts were also examined. The results showed that the n-hexane extract of Coriolus versicolor had the strongest anti-alpha-amylase activity, while the n-hexane extract of Grifola   frondosa showed the most potent anti-alpha-glucosidase activity. Compared with acarbose, the anti-alpha-amylase activity of all mushroom extracts was weaker, however a stronger anti-alpha-glucosidase activity was noted. GC-MS analysis showed that the magnitude of potency of inhibiting alpha-glucosidase activity varied with the levels of oleic acid and linoleic acid present in the extracts. These findings were consistent with the IC50 values of these free fatty acids on   inhibiting alpha-glucosidase activity. Taken together, this study suggests that oleic acid and linoleic acid could have contributed to the potent anti-alpha-glucosidase activity of selected medicinal mushrooms.
{Author Address}: Department of Agricultural Chemistry, National Taiwan University, No. 1, Sec. 4,   Roosevelt Road, Taipei 106, Taiwan. nglt97@ntu.edu.tw.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Sillo, Fabiano; Gissi, Carmela; Chignoli, Daniele; Ragni, Enrico; Popolo, Laura; Balestrini, Raffaella
{Year}: 2013
{Title}: Expression and phylogenetic analyses of the Gel/Gas proteins of Tuber melanosporum provide insights into the function and evolution of glucan remodeling enzymes in fungi
{URL}: http://www.sciencedirect.com/science/article/pii/S1087184513000273
{Tag}: 0
{Star}: 0
{Journal}: Fungal Genetics and Biology
{Volume}: 53
{Issue}: 0
{Pages}: 10-21
{Date Displayed}: 2013/4//
{Alternate Title}: Fungal Genetics and Biology
{ISBN/ISSN}: 1087-1845
{Keywords}: Mycorrhizal fungi; GH72 family; Glucanosyltransferases; Cell wall; Fruiting body; Tuber melanosporum
{Abstract}: The β(1,3)-glucanosyltransferases of the GH72 family are redundant enzymes that are essential for the formation and dynamic remodeling of the fungal wall during different stages of the life cycle. Four putative genes encoding glycosylphosphatidylinositol (GPI)-anchored β(1,3)-glucanosyltransferases, designated TmelGEL1, TmelGEL2, TmelGEL4 and TmelGAS4, have been annotated in the genome of Tuber melanosporum, an ectomycorrhizal fungus that also produces a hypogeous fruiting body (FB) of great commercial value (black truffle). This work focuses on the characterization and expression of this multigene family by taking advantage of a laser microdissection (LMD) technology that has been used to separate two distinct compartments in the FB, the hyphae and the asci containing the ascospores. Of the four genes, TmelGEL1 was the most up-regulated in the FB compared to the free-living mycelium. Inside the FB, the expression of TmelGEL1 was restricted to the hyphal compartment. A phylogenetic analysis of the Gel/Gas protein family of T. melanosporum was also carried out. A total of 237 GH72 proteins from 51 Ascomycotina and 3 Basidiomycota (outgroup) species were analyzed. The resulting tree provides insight into the evolution of the T. melanosporum proteins and identifies new GH72 paralogs/subfamilies. Moreover, it represents a starting point to formulate new hypotheses on the significance of the striking GH72 gene redundancy in fungal biology.